Y1112_STRPN
ID Y1112_STRPN Reviewed; 279 AA.
AC Q97QT7;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DegV domain-containing protein SP_1112;
GN OrderedLocusNames=SP_1112;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and may
CC play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
CC -!- INTERACTION:
CC Q97QT7; A0A0H2UPN3: SP_0859; NbExp=2; IntAct=EBI-6474517, EBI-6474523;
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DR EMBL; AE005672; AAK75223.1; -; Genomic_DNA.
DR PIR; F95128; F95128.
DR RefSeq; WP_000161399.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97QT7; -.
DR SMR; Q97QT7; -.
DR IntAct; Q97QT7; 1.
DR STRING; 170187.SP_1112; -.
DR EnsemblBacteria; AAK75223; AAK75223; SP_1112.
DR KEGG; spn:SP_1112; -.
DR eggNOG; COG1307; Bacteria.
DR OMA; EIHAKIN; -.
DR PhylomeDB; Q97QT7; -.
DR BioCyc; SPNE170187:G1FZB-1137-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1180.10; -; 1.
DR InterPro; IPR003797; DegV.
DR InterPro; IPR043168; DegV_C.
DR Pfam; PF02645; DegV; 1.
DR TIGRFAMs; TIGR00762; DegV; 1.
DR PROSITE; PS51482; DEGV; 1.
PE 1: Evidence at protein level;
KW Lipid-binding.
FT CHAIN 1..279
FT /note="DegV domain-containing protein SP_1112"
FT /id="PRO_0000209795"
FT DOMAIN 4..277
FT /note="DegV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT BINDING 62
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT BINDING 94
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ SEQUENCE 279 AA; 30658 MW; 767394119DC89CAE CRC64;
MTKIKIVTDS SVTIEPELVK QLDITIVPLS VMIDNVVYSD ADLKEEGKFL QLMQESKNLP
KTSQPPVGVF AEIFEDLCKD GGQILAIHMS HALSGTVEAA RQGASLSTAD VTVVDSSFTD
QALKFQVVEA AKLAQEGKDM EAILSHVEEV KNHTELYIGV STLENLVKGG RISRVTGLLS
SLLNIRAVMQ MKDHELQPMV KGRGTKTFKK WLDELITSLS ERAVAEIGIS YSGSDDWAKE
MKESLQAYVE KPISVLETGS IIQTHTGENA WAILIRYHS